Literature DB >> 16482244

PELDOR study on the tyrosyl radicals in the R2 protein of mouse ribonucleotide reductase.

Daniele Biglino1, Peter P Schmidt, Edward J Reijerse, Wolfgang Lubitz.   

Abstract

Pulse electron-electron double resonance (PELDOR) has been employed to measure the distance between the putative tyrosyl radicals in the two halves of the R2 subunit from mouse ribonucleotide reductase. The results provide experimental evidence that the active, tyrosyl radical containing mouse R2 subunit forms a homodimeric form in solution. The distance between the two tyrosyl radicals present in the dimer was determined to be 3.25 +/- 0.05 nm.

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Year:  2005        PMID： 16482244     DOI： 10.1039/b513950c

Source DB:  PubMed          Journal:  Phys Chem Chem Phys        ISSN： 1463-9076            Impact factor:   3.676


  3 in total

1.  High-field pulsed electron-electron double resonance spectroscopy to determine the orientation of the tyrosyl radicals in ribonucleotide reductase.

Authors:  V P Denysenkov; T F Prisner; J Stubbe; M Bennati
Journal:  Proc Natl Acad Sci U S A       Date:  2006-08-28       Impact factor: 11.205

2.  Equilibration of tyrosyl radicals (Y356•, Y731•, Y730•) in the radical propagation pathway of the Escherichia coli class Ia ribonucleotide reductase.

Authors:  Kenichi Yokoyama; Albert A Smith; Björn Corzilius; Robert G Griffin; Joanne Stubbe
Journal:  J Am Chem Soc       Date:  2011-10-26       Impact factor: 15.419

3.  Direct Measurement of the Radical Translocation Distance in the Class I Ribonucleotide Reductase from Chlamydia trachomatis.

Authors:  Jovan Livada; Ryan J Martinie; Laura M K Dassama; Carsten Krebs; J Martin Bollinger; Alexey Silakov
Journal:  J Phys Chem B       Date:  2015-06-30       Impact factor: 2.991
  3 in total

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